RUTF_ECOLI
ID RUTF_ECOLI Reviewed; 164 AA.
AC P75893;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=FMN reductase (NADH) RutF;
DE EC=1.5.1.42;
DE AltName: Full=FMN reductase;
DE AltName: Full=NADH-flavin reductase RutF;
DE AltName: Full=NADH:flavin oxidoreductase;
GN Name=rutF; Synonyms=ycdH; OrderedLocusNames=b1007, JW5138;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION.
RX PubMed=11121068; DOI=10.1073/pnas.97.26.14674;
RA Zimmer D.P., Soupene E., Lee H.L., Wendisch V.F., Khodursky A.B.,
RA Peter B.J., Bender R.A., Kustu S.;
RT "Nitrogen regulatory protein C-controlled genes of Escherichia coli:
RT scavenging as a defense against nitrogen limitation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14674-14679(2000).
RN [5]
RP FUNCTION IN PYRIMIDINE CATABOLISM, AND NOMENCLATURE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16540542; DOI=10.1073/pnas.0600521103;
RA Loh K.D., Gyaneshwar P., Markenscoff Papadimitriou E., Fong R., Kim K.-S.,
RA Parales R., Zhou Z., Inwood W., Kustu S.;
RT "A previously undescribed pathway for pyrimidine catabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5114-5119(2006).
RN [6]
RP INDUCTION.
RX PubMed=17919280; DOI=10.1111/j.1365-2958.2007.05954.x;
RA Shimada T., Hirao K., Kori A., Yamamoto K., Ishihama A.;
RT "RutR is the uracil/thymine-sensing master regulator of a set of genes for
RT synthesis and degradation of pyrimidines.";
RL Mol. Microbiol. 66:744-757(2007).
RN [7]
RP REACTION MECHANISM, AND CATALYTIC ACTIVITY.
RX PubMed=20369853; DOI=10.1021/ja9107676;
RA Mukherjee T., Zhang Y., Abdelwahed S., Ealick S.E., Begley T.P.;
RT "Catalysis of a flavoenzyme-mediated amide hydrolysis.";
RL J. Am. Chem. Soc. 132:5550-5551(2010).
RN [8]
RP FUNCTION AS A FLAVIN REDUCTASE, AND DISRUPTION PHENOTYPE.
RX PubMed=20400551; DOI=10.1128/jb.00201-10;
RA Kim K.S., Pelton J.G., Inwood W.B., Andersen U., Kustu S., Wemmer D.E.;
RT "The Rut pathway for pyrimidine degradation: novel chemistry and toxicity
RT problems.";
RL J. Bacteriol. 192:4089-4102(2010).
CC -!- FUNCTION: Catalyzes the reduction of FMN to FMNH2 which is used to
CC reduce pyrimidine by RutA via the Rut pathway. In vitro, the flavin
CC reductase Fre can substitute for the function of RutF, however, RutF is
CC required for uracil utilization in vivo. {ECO:0000269|PubMed:16540542,
CC ECO:0000269|PubMed:20400551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.42;
CC Evidence={ECO:0000269|PubMed:20369853};
CC -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC called GlnG) and repressed by RutR. {ECO:0000269|PubMed:11121068,
CC ECO:0000269|PubMed:17919280}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on uridine
CC as the sole source of nitrogen at room temperature.
CC {ECO:0000269|PubMed:20400551}.
CC -!- MISCELLANEOUS: The Rut pathway degrades exogenous pyrimidines as the
CC sole nitrogen source at room temperature but not at 37 degrees Celsius,
CC a restriction that is apparently a consequence of an inadequate ability
CC to remove toxic malonic semialdehyde at the higher temperature
CC (RutE/YdfG function).
CC -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC RutF subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74092.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35774.2; -; Genomic_DNA.
DR PIR; E64842; E64842.
DR RefSeq; NP_415527.4; NC_000913.3.
DR RefSeq; WP_001028083.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P75893; -.
DR SMR; P75893; -.
DR BioGRID; 4259548; 7.
DR STRING; 511145.b1007; -.
DR PaxDb; P75893; -.
DR PRIDE; P75893; -.
DR EnsemblBacteria; AAC74092; AAC74092; b1007.
DR EnsemblBacteria; BAA35774; BAA35774; BAA35774.
DR GeneID; 946594; -.
DR KEGG; ecj:JW5138; -.
DR KEGG; eco:b1007; -.
DR PATRIC; fig|1411691.4.peg.1264; -.
DR EchoBASE; EB3614; -.
DR eggNOG; COG1853; Bacteria.
DR HOGENOM; CLU_059021_2_2_6; -.
DR InParanoid; P75893; -.
DR OMA; WFDRGYH; -.
DR PhylomeDB; P75893; -.
DR BioCyc; EcoCyc:G6518-MON; -.
DR BioCyc; MetaCyc:G6518-MON; -.
DR PRO; PR:P75893; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0052874; F:FMN reductase (NADH) activity; IDA:EcoCyc.
DR GO; GO:0008752; F:FMN reductase activity; IEA:InterPro.
DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0019740; P:nitrogen utilization; IDA:UniProtKB.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IMP:EcoCyc.
DR GO; GO:0006212; P:uracil catabolic process; IDA:UniProtKB.
DR Gene3D; 2.30.110.10; -; 1.
DR HAMAP; MF_00833; RutF; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR019917; RutF.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
DR TIGRFAMs; TIGR03615; RutF; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..164
FT /note="FMN reductase (NADH) RutF"
FT /id="PRO_0000085537"
SQ SEQUENCE 164 AA; 17749 MW; 70C0FDFF45183764 CRC64;
MNIVDQQTFR DAMSCMGAAV NIITTDGPAG RAGFTASAVC SVTDTPPTLL VCLNRGASVW
PAFNENRTLC VNTLSAGQEP LSNLFGGKTP MEHRFAAARW QTGVTGCPQL EEALVSFDCR
ISQVVSVGTH DILFCAIEAI HRHTTPYGLV WFDRSYHALM RPAC
